| UniProt ID | PRS10_YEAST | |
|---|---|---|
| UniProt AC | P53549 | |
| Protein Name | 26S proteasome subunit RPT4 | |
| Gene Name | RPT4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 437 | |
| Subcellular Localization | ||
| Protein Description | The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).. | |
| Protein Sequence | MSEEQDPLLAGLGETSGDNHTQQSHEQQPEQPQETEEHHEEEPSRVDPEQEAHNKALNQFKRKLLEHRRYDDQLKQRRQNIRDLEKLYDKTENDIKALQSIGQLIGEVMKELSEEKYIVKASSGPRYIVGVRNSVDRSKLKKGVRVTLDITTLTIMRILPRETDPLVYNMTSFEQGEITFDGIGGLTEQIRELREVIELPLKNPEIFQRVGIKPPKGVLLYGPPGTGKTLLAKAVAATIGANFIFSPASGIVDKYIGESARIIREMFAYAKEHEPCIIFMDEVDAIGGRRFSEGTSADREIQRTLMELLTQMDGFDNLGQTKIIMATNRPDTLDPALLRPGRLDRKVEIPLPNEAGRLEIFKIHTAKVKKTGEFDFEAAVKMSDGFNGADIRNCATEAGFFAIRDDRDHINPDDLMKAVRKVAEVKKLEGTIEYQKL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSEEQDPLL ------CCCCCCCCC | 50.25 | 12504901 | |
| 63 | Ubiquitination | ALNQFKRKLLEHRRY HHHHHHHHHHHHHCH | 59.00 | 17644757 | |
| 75 | Ubiquitination | RRYDDQLKQRRQNIR HCHHHHHHHHHHHHH | 35.80 | 23749301 | |
| 86 | Acetylation | QNIRDLEKLYDKTEN HHHHHHHHHHHCCHH | 60.69 | 24489116 | |
| 100 | Phosphorylation | NDIKALQSIGQLIGE HHHHHHHHHHHHHHH | 29.54 | 19795423 | |
| 116 | Acetylation | MKELSEEKYIVKASS HHHHCCCCEEEECCC | 35.90 | 24489116 | |
| 202 | Acetylation | EVIELPLKNPEIFQR HHHCCCCCCHHHHHH | 69.39 | 24489116 | |
| 202 | Ubiquitination | EVIELPLKNPEIFQR HHHCCCCCCHHHHHH | 69.39 | 17644757 | |
| 216 | Ubiquitination | RVGIKPPKGVLLYGP HCCCCCCCCEEEECC | 70.90 | 17644757 | |
| 228 | Ubiquitination | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 22817900 | |
| 233 | Ubiquitination | TGKTLLAKAVAATIG CCHHHHHHHHHHHHC | 43.28 | 22817900 | |
| 292 | Phosphorylation | AIGGRRFSEGTSADR CCCCCCCCCCCCHHH | 33.05 | 17563356 | |
| 346 | Ubiquitination | RPGRLDRKVEIPLPN CCCCCCCEEEECCCC | 43.84 | 17644757 | |
| 362 | Acetylation | AGRLEIFKIHTAKVK CCCEEEEEEEECEEE | 38.96 | 24489116 | |
| 362 | Ubiquitination | AGRLEIFKIHTAKVK CCCEEEEEEEECEEE | 38.96 | 17644757 | |
| 417 | Acetylation | INPDDLMKAVRKVAE CCHHHHHHHHHHHHH | 51.53 | 24489116 | |
| 427 | Ubiquitination | RKVAEVKKLEGTIEY HHHHHHHHHCCCEEE | 57.87 | 22106047 | |
| 436 | Ubiquitination | EGTIEYQKL------ CCCEEEECC------ | 56.09 | 23749301 | |
| 436 | Acetylation | EGTIEYQKL------ CCCEEEECC------ | 56.09 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PRS10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRS10_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PRS10_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "N-terminal modifications of the 19S regulatory particle subunits ofthe yeast proteasome."; Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.; Arch. Biochem. Biophys. 409:341-348(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASSSPECTROMETRY. | |
